Title: Crucial Role for the VWF A1 Domain In Binding to Type IV Collagen Short title: VWF Binds Collagen IV

نویسندگان

  • Veronica H. Flood
  • Abraham C. Schlauderaff
  • Sandra L. Haberichter
  • Tricia L. Slobodianuk
  • Paula M. Jacobi
  • Daniel B. Bellissimo
  • Pamela A. Christopherson
  • Kenneth D. Friedman
  • Joan Cox Gill
  • Raymond G. Hoffmann
  • Robert R. Montgomery
چکیده

Department of Pediatrics, Division of Hematology/Oncology, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI 53226 Children’s Research Institute, Children’s Hospital of Wisconsin, Milwaukee, WI 53226 Blood Research Institute, BloodCenter of Wisconsin, 8727 Watertown Plank Rd, Milwaukee, WI 53226 Department of Pediatrics, Division of Quantitative Health Sciences, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI 53226

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منابع مشابه

Regular Article THROMBOSIS AND HEMOSTASIS Crucial role for the VWF A1 domain in binding to type IV collagen

• Collagen 4 binds to the VWF A1 domain, and this binding is reduced or abrogated by select VWF A1 domain sequence variations. • Platelet binding to collagen 4 under flow conditions is dependent on the presence of VWF. Von Willebrand factor (VWF) contains binding sites for platelets and for vascular collagens to facilitate clot formation at sites of injury. Although previous work has shown that...

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Crucial role for the VWF A1 domain in binding to type IV collagen.

Von Willebrand factor (VWF) contains binding sites for platelets and for vascular collagens to facilitate clot formation at sites of injury. Although previous work has shown that VWF can bind type IV collagen (collagen 4), little characterization of this interaction has been performed. We examined the binding of VWF to collagen 4 in vitro and extended this characterization to a murine model of ...

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von Willebrand factor binds to native collagen VI primarily via its A1 domain.

Collagen VI is abundant in the arterial subendothelium. To investigate its mechanism of interaction with von Willebrand factor (vWF), collagen VI was isolated from human placenta and from the extracellular matrix of the human lung fibroblast cell line MRC-5. Purified vWF bound to non-digested collagen VI with moderately high affinity (EC50 approximately 5 nM) and could be inhibited by the Hirud...

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Regular Article THROMBOSIS AND HEMOSTASIS Analysis of the role of von Willebrand factor, platelet glycoprotein VI-, and a2b1-mediated collagen binding in thrombus formation

von Willebrand factor (VWF) plays an important role in coagulation as a carrier protein for factor VIII (FVIII) and in primary hemostasis with binding of VWF to exposed subendothelial collagens. The most hemostatically important forms of collagen include the fibrillar collagens I and III, and the microfibrillar collagen VI. VWF binds to collagen I and III via theVWFA1andA3domainswhereas only th...

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Role of the glycoprotein Ib-binding A1 repeat and the RGD sequence in platelet adhesion to human recombinant von Willebrand factor.

To assess the relative importance of the glycoprotein (GP) Ib binding domain and the RGDS binding site in platelet adhesion to isolated von Willebrand factor (vWF) and to collagen preincubated with vWF, we deleted the A1 domain yielding delta A1-vWF and introduced an aspartate-to-glycine substitution in the RGDS sequence by site-directed mutagenesis (RGGS-vWF). Recombinant delta A1-vWF and RGGS...

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تاریخ انتشار 2015